[1]	NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF ARG-385, AND INDUCTION. PubMed=10979956 [NCBI, ExPASy, EBI, Israel, Japan] Kawashima T., Hirose K., Satoh T., Kaneko A., Ikeda Y., Kaziro Y., Nosaka T., Kitamura T.; "MgcRacGAP is involved in the control of growth and differentiation of hematopoietic cells."; Blood 96:2116-2124(2000).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Testis; DOI=10.1101/gr.GR1547R; PubMed=11230166 [NCBI, ExPASy, EBI, Israel, Japan] Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.; "Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."; Genome Res. 11:422-435(2001).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Hepatoma; DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan] Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; "Complete sequencing and characterization of 21,243 full-length human cDNAs."; Nat. Genet. 36:40-45(2004).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."; Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Placenta, and Testis; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 63-632. TISSUE=Brain; DOI=10.1093/dnares/7.2.143; PubMed=10819331 [NCBI, ExPASy, EBI, Israel, Japan] Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."; DNA Res. 7:143-150(2000).
[7]	FUNCTION, AND TISSUE SPECIFICITY. DOI=10.1074/jbc.273.11.6019; PubMed=9497316 [NCBI, ExPASy, EBI, Israel, Japan] Toure A., Dorseuil O., Morin L., Timmons P., Jegou B., Reibel L., Gacon G.; "MgcRacGAP, a new human GTPase-activating protein for Rac and Cdc42 similar to Drosophila rotundRacGAP gene product, is expressed in male germ cells."; J. Biol. Chem. 273:6019-6023(1998).
[8]	FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DOMAIN. DOI=10.1074/jbc.M007252200; PubMed=11085985 [NCBI, ExPASy, EBI, Israel, Japan] Hirose K., Kawashima T., Iwamoto I., Nosaka T., Kitamura T.; "MgcRacGAP is involved in cytokinesis through associating with mitotic spindle and midbody."; J. Biol. Chem. 276:5821-5828(2001).
[9]	FUNCTION, INTERACTION WITH SLC26A8, AND TISSUE SPECIFICITY. DOI=10.1074/jbc.M011740200; PubMed=11278976 [NCBI, ExPASy, EBI, Israel, Japan] Toure A., Morin L., Pineau C., Becq F., Dorseuil O., Gacon G.; "Tat1, a novel sulfate transporter specifically expressed in human male germ cells and potentially linked to rhogtpase signaling."; J. Biol. Chem. 276:20309-20315(2001).
[10]	INTERACTION WITH RND2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. DOI=10.1042/BJ20021652; PubMed=12590651 [NCBI, ExPASy, EBI, Israel, Japan] Naud N., Toure A., Liu J., Pineau C., Morin L., Dorseuil O., Escalier D., Chardin P., Gacon G.; "Rho family GTPase Rnd2 interacts and co-localizes with MgcRacGAP in male germ cells."; Biochem. J. 372:105-112(2003).
[11]	INTERACTION WITH AURKB, AND PHOSPHORYLATION AT SER-387. DOI=10.1016/S1534-5807(03)00089-3; PubMed=12689593 [NCBI, ExPASy, EBI, Israel, Japan] Minoshima Y., Kawashima T., Hirose K., Tonozuka Y., Kawajiri A., Bao Y.C., Deng X., Tatsuka M., Narumiya S., May W.S. Jr., Nosaka T., Semba K., Inoue T., Satoh T., Inagaki M., Kitamura T.; "Phosphorylation by aurora B converts MgcRacGAP to a RhoGAP during cytokinesis."; Dev. Cell 4:549-560(2003).
[12]	FUNCTION, AND MUTAGENESIS OF ARG-385. DOI=10.1016/j.yexcr.2003.10.015; PubMed=14729465 [NCBI, ExPASy, EBI, Israel, Japan] Lee J.S., Kamijo K., Ohara N., Kitamura T., Miki T.; "MgcRacGAP regulates cortical activity through RhoA during cytokinesis."; Exp. Cell Res. 293:275-282(2004).
[13]	INTERACTION WITH PRC1. DOI=10.1074/jbc.M313257200; PubMed=14744859 [NCBI, ExPASy, EBI, Israel, Japan] Ban R., Irino Y., Fukami K., Tanaka H.; "Human mitotic spindle-associated protein PRC1 inhibits MgcRacGAP activity toward Cdc42 during the metaphase."; J. Biol. Chem. 279:16394-16402(2004).
[14]	FUNCTION, INTERACTION WITH ECT2, AND SUBCELLULAR LOCATION. DOI=10.1073/pnas.0504145102; PubMed=16129829 [NCBI, ExPASy, EBI, Israel, Japan] Zhao W.-M., Fang G.; "MgcRacGAP controls the assembly of the contractile ring and the initiation of cytokinesis."; Proc. Natl. Acad. Sci. U.S.A. 102:13158-13163(2005).
[15]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161; SER-164; SER-203 AND SER-206, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).
[16]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan] Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."; Nat. Biotechnol. 24:1285-1292(2006).
[17]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161; SER-164; SER-170; SER-203; SER-214; THR-342; THR-580; THR-588; SER-590 AND SER-628, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1073/pnas.0507066103; PubMed=16565220 [NCBI, ExPASy, EBI, Israel, Japan] Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; "Phosphoproteome analysis of the human mitotic spindle."; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
[18]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-606 AND SER-628, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan] Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; J. Proteome Res. 6:4150-4162(2007).
[19]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185 AND SER-187, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan] Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).

Comments

FUNCTION: Essential for the early stages of embryogenesis and may play a role in the microtubule-dependent steps in cytokinesis. Plays key roles in controlling cell growth and differentiation of hematopoietic cells through mechanisms other than regulating Rac GTPase activity. Also involved in the regulation of growth-related processes in adipocytes and myoblasts. May be involved in regulating spermatogenesis and in the RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase activation) activity towards CDC42 and RAC1 and less towards RHOA. Required for initiation of cleavage furrow ingression by regulating ECT2 and for assembly of the contractile ring. May play a role in regulating cortical activity through RHOA during cytokinesis. May participate in the regulation of sulfate transport in male germ cells.
SUBUNIT: Associates with alpha-, beta- and gamma-tubulin and microtubules. Interacts via its Rho-GAP domain with RND2. Associates with AURKB during M phase. Interacts via its Rho-GAP domain and basic region with PRC1. The interaction with PRC1 inhibits its GAP activity towards CDC42 in vitro, which may be required for maintaining normal spindle morphology. Associates with ECT2 at anaphase and during cytokinesis. Interacts with SLC26A8 via its N-terminus.
INTERACTION:
P31946:YWHAB; NbExp=1; IntAct=EBI-717233, EBI-359815;
P61981:YWHAG; NbExp=1; IntAct=EBI-717233, EBI-359832;
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Spindle. Acrosome. Note=During interphase, localized to the nucleus and cytoplasm along with microtubules, in anaphase, is redistributed to the central spindle and, in telophase and cytokinesis, to the midbody. Colocalizes with RHOA at the contractile ring during cytokinesis. Colocalizes with RND2 in Golgi-derived proacrosomal vesicles and the acrosome.
TISSUE SPECIFICITY: Highly expressed in testis, thymus and placenta. Expressed at lower levels in spleen and peripheral blood lymphocytes. In testis, expression is restricted to germ cells with the highest levels of expression found in spermatocytes. Expression is regulated in a cell cycle-dependent manner and peaks during G2/M phase.
INDUCTION: Expression is down-regulated during macrophage differention of HL-60 cells.
DOMAIN: The coiled coil region is indispensible for localization to the midbody during cytokinesis.
PTM: Phosphorylated at multiple sites in the midbody during cytokinesis. Phosphorylation by AURKB on SER-387 at the midbody is, at least in part, responsible for exerting its latent GAP activity towards RhoA.
SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
SIMILARITY: Contains 1 Rho-GAP domain.
SEQUENCE CAUTION:
- Sequence=AAH24144.1; Type=Frameshift; Positions=171, 205, 437;

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AB030251; BAA90247.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136794; CAB66728.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK000733; BAA91347.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR533565; CAG38596.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC024144; AAH24144.1; ALT_FRAME; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC032754; AAH32754.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB040911; BAA96002.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

D59430; D59430.

RefSeq

NP_001119575.1; -.
NP_001119576.1; -.
NP_037409.2; -.

UniGene

Hs.505469

3D structure databases

PDB

2OVJ; X-ray; 1.49 A; A=348-546.

[ExPASy / RCSB / EBI]

PDBsum

2OVJ; -.

ModBase

Q9H0H5.

Protein-protein interaction databases

IntAct

Q9H0H5; -.

PTM databases

PhosphoSite

Q9H0H5; -.

Enzyme and pathway databases

Reactome

REACT_11044; Signaling by Rho GTPases.

Organism-specific databases

H-InvDB

HIX0036723; -.

HGNC

HGNC:9804; RACGAP1.

GeneLynx

RACGAP1; Homo sapiens.

GenAtlas

RACGAP1.

MIM

604980; gene. [NCBI / EBI]

PA34165; -.

Gene expression databases

ArrayExpress

Q9H0H5; -.

CleanEx

HS_RACGAP1; -.

GermOnline

ENSG00000161800; Homo sapiens.

Ontologies

GO:0005634;	Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0043014;	Molecular function: alpha-tubulin binding (inferred from direct assay from UniProtKB).
GO:0048487;	Molecular function: beta-tubulin binding (inferred from direct assay from UniProtKB).
GO:0043015;	Molecular function: gamma-tubulin binding (inferred from direct assay from UniProtKB).
GO:0005096;	Molecular function: GTPase activator activity (inferred from direct assay from UniProtKB).
GO:0008022;	Molecular function: protein C-terminus binding (inferred from physical interaction from UniProtKB).
GO:0000915;	Biological process: cytokinesis, contractile ring formation (inferred from mutant phenotype from UniProtKB).
GO:0007108;	Biological process: cytokinesis, initiation of separation (inferred from mutant phenotype from UniProtKB).
GO:0009790;	Biological process: embryonic development (inferred from sequence or structural similarity from UniProtKB).
GO:0007405;	Biological process: neuroblast proliferation (inferred from sequence or structural similarity from UniProtKB).
GO:0007283;	Biological process: spermatogenesis (inferred from expression pattern from UniProtKB).
GO:0008272;	Biological process: sulfate transport (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR002219; DAG_PE_bd.
IPR000198; RhoGAP.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.555.10; RhoGAP; 1.

Pfam

PF00130; C1_1; 1.
PF00620; RhoGAP; 1.
Pfam graphical view of domain structure.

SMART

SM00109; C1; 1.
SM00324; RhoGAP; 1.
SMART graphical view of domain structure.

PROSITE

PS50238; RHOGAP; 1.
PS00479; ZF_DAG_PE_1; 1.
PS50081; ZF_DAG_PE_2; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q9H0H5.

Proteomic databases

PeptideAtlas

Q9H0H5; -.

Genome annotation databases

Ensembl

ENSG00000161800; Homo sapiens. [Contig view]

GeneID

29127; -.

KEGG

hsa:29127; -.

Phylogenomic databases

HOGENOM

Q9H0H5; -.

HOVERGEN

Q9H0H5; -.

Other

LinkHub

Q9H0H5; -.

SOURCE

RACGAP1; Homo sapiens.

ProtoNet

Q9H0H5.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cell cycle; Cell division; Coiled coil; Cytoplasm; Developmental protein; Differentiation; GTPase activation; Ion transport; Metal-binding; Microtubule; Nucleus; Phorbol-ester binding; Phosphoprotein; Spermatogenesis; Transport; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 632`	`632`	`Rac GTPase-activating protein 1.`	`PRO_0000228808`
`DOMAIN`	`349 539`	`191`	`Rho-GAP.`
`ZN_FING`	`286 335`	`50`	`Phorbol-ester/DAG-type.`
`REGION`	`1 180`	`180`	`Interaction with SLC26A8.`
`COILED`	`53 110`	`58`	`Potential.`
`MOD_RES`	`161 161`		`Phosphothreonine.`
`MOD_RES`	`164 164`		`Phosphoserine.`
`MOD_RES`	`170 170`		`Phosphoserine.`
`MOD_RES`	`185 185`		`Phosphoserine.`
`MOD_RES`	`187 187`		`Phosphoserine.`
`MOD_RES`	`203 203`		`Phosphoserine.`
`MOD_RES`	`206 206`		`Phosphoserine.`
`MOD_RES`	`214 214`		`Phosphoserine.`
`MOD_RES`	`342 342`		`Phosphothreonine.`
`MOD_RES`	`387 387`		`Phosphoserine.`
`MOD_RES`	`580 580`		`Phosphothreonine.`
`MOD_RES`	`588 588`		`Phosphothreonine.`
`MOD_RES`	`590 590`		`Phosphoserine.`
`MOD_RES`	`606 606`		`Phosphothreonine.`
`MOD_RES`	`628 628`		`Phosphoserine.`
`MUTAGEN`	`385 385`		`R->A: Abolishes GAP activity towards RAC1 and CDC42 and induces multiple blebs during cytokinesis.`
`CONFLICT`	`155 155`		`D -> H (in Ref. 3; BAA91347).`
`CONFLICT`	`518 518`		`L -> S (in Ref. 1; BAA90247).`
`HELIX`	`351 354`	`4`
`STRAND`	`357 360`	`4`
`HELIX`	`364 376`	`13`
`TURN`	`377 379`	`3`
`TURN`	`381 385`	`5`
`HELIX`	`390 401`	`12`
`HELIX`	`409 411`	`3`
`HELIX`	`415 427`	`13`
`STRAND`	`429 431`	`3`
`TURN`	`436 438`	`3`
`HELIX`	`439 447`	`9`
`HELIX`	`451 463`	`13`
`HELIX`	`467 485`	`19`
`HELIX`	`493 504`	`12`
`STRAND`	`508 511`	`4`
`HELIX`	`514 533`	`20`
`HELIX`	`536 540`	`5`
`HELIX`	`541 543`	`3`

Sequence information

Length: 632 AA [This is the length of the unprocessed precursor]

Molecular weight: 71027 Da [This is the MW of the unprocessed precursor]

CRC64: 032B7DF9CEA8F39D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDTMMLNVRN LFEQLVRRVE ILSEGNEVQF IQLAKDFEDF RKKWQRTDHE LGKYKDLLMK 

        70         80         90        100        110        120 
AETERSALDV KLKHARNQVD VEIKRRQRAE ADCEKLERQI QLIREMLMCD TSGSIQLSEE 

       130        140        150        160        170        180 
QKSALAFLNR GQPSSSNAGN KRLSTIDESG SILSDISFDK TDESLDWDSS LVKTFKLKKR 

       190        200        210        220        230        240 
EKRRSTSRQF VDGPPGPVKK TRSIGSAVDQ GNESIVAKTT VTVPNDGGPI EAVSTIETVP 

       250        260        270        280        290        300 
YWTRSRRKTG TLQPWNSDST LNSRQLEPRT ETDSVGTPQS NGGMRLHDFV SKTVIKPESC 

       310        320        330        340        350        360 
VPCGKRIKFG KLSLKCRDCR VVSHPECRDR CPLPCIPTLI GTPVKIGEGM LADFVSQTSP 

       370        380        390        400        410        420 
MIPSIVVHCV NEIEQRGLTE TGLYRISGCD RTVKELKEKF LRVKTVPLLS KVDDIHAICS 

       430        440        450        460        470        480 
LLKDFLRNLK EPLLTFRLNR AFMEAAEITD EDNSIAAMYQ AVGELPQANR DTLAFLMIHL 

       490        500        510        520        530        540 
QRVAQSPHTK MDVANLAKVF GPTIVAHAVP NPDPVTMLQD IKRQPKVVER LLSLPLEYWS 

       550        560        570        580        590        600 
QFMMVEQENI DPLHVIENSN AFSTPQTPDI KVSLLGPVTT PEHQLLKTPS SSSLSQRVRS 

       610        620        630 
TLTKNTPRFG SKSKSATNLG RQGNFFASPM LK

Q9H0H5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools